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A Study of the Activities of Carbohydrate-Metabolizing Enzymes and the Levels of Carbohydrate Metabolites and Amino Acids in Normal Liver and in Hepatocellular Carcinoma

  • U. Gerbracht
  • E. Roth
  • K. Becker
  • M. Reinacher
  • E. Eigenbrodt

Abstract

Primary hepatocellular carcinoma was induced by treatment with the initiator N’nitrosomorpholine followed by the promoting agents phenobarbital or Clofibrate. In those tumors, the activities of pyruvate kinase, fructose 1,6-bisphosphatase and lactate dehydrogenase were reduced. A reduction in the activities of pyruvate kinase and fructose 1,6-bisphosphatase along with an increase in malic enzyme activity were observed in the host livers of tumor-bearing rats and in livers of rats pretreated with the promoter alone, suggesting that these changes may be a general effect of the xenobiotic which serves as the tumor promoter in chemical-induced hepatocarcinogenesis. Such changes were independent of the promoter used, whereas alterations in the enzymes gamma-glutamyltransferase and glucose 6-phosphate dehydrogenase were dependent on the promoter type. Enolase activity was not affected by any treatment. In a second experiment, relevant carbohydrate metabolites, amino acid levels and selected carbohydrate metabolizing enzyme activities were determined in hepatic tumors from rats which had received phenobarbital as the promoting drug. Serine dehydratase and glucose 6-phosphatase were strongly depressed when compared to host livers and livers from rats treated only with N’nitrosomorpholine. On the other hand, glucokinase activity was reduced in tumors as well as in host livers of tumor-bearing rats, while phosphofructokinase and 6-phosphogluconate dehydrogenase activities were unaltered in all livers. The decrease in pyruvate kinase, fructose 1,6-bisphosphatase, serine dehydratase and the subsequent decrease in pyruvate and alanine in hepatocellular carcinoma were positively correlated with an increase in fructose 1,6-bisphosphate and glycine.

Keywords

Pyruvate Kinase Malic Enzyme Primary Hepatocellular Carcinoma Host Liver Pyruvate Kinase Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • U. Gerbracht
    • 1
  • E. Roth
    • 2
  • K. Becker
    • 3
  • M. Reinacher
    • 4
  • E. Eigenbrodt
    • 1
  1. 1.Institut für Biochemie und EndokrinologieGermany
  2. 2.Chirurgische UniversitätsklinikWienAustria
  3. 3.Institut für Veterinär-PhysiologieGermany
  4. 4.Institut für Veterinär-PathologieGermany

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